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Submitted on April 17, 2002
Revised on May 29, 2002
Accepted on June 20, 2002

A proteomics approach for the identification of DNA binding activities observed in the electrophoretic mobility shift assay

Andrew J. Woo, James S. Dods, Evelyn Susanto, Daniela Ulgiati, and Lawrence J. Abraham

Biochemistry & Molecular Biology, School of Biomedical & Chemical Sciences, University of Western Australia, Crawley, Western Australia 6009

Corresponding Author: Labraham{at}cyllene.uwa.edu.au

Transcription factors lie at the centre of gene regulation and their identification is crucial to the understanding of transcription and gene expression. Traditionally, the isolation and identification of transcription factors has been a long and laborious task. We present here a novel method for the identification of DNA binding proteins seen in the electrophoretic mobility shift assay (EMSA) using the power of two dimensional electrophoresis coupled with mass spectrometry. By coupling SDS-PAGE and IEF to EMSA, the molecular weight (MW) and pI of a protein complex seen in EMSA were estimated. Candidate proteins were then identified on a two-dimensional array at the predetermined pI and MW coordinates and identified by mass spectrometry. We show here, the successful isolation of a functionally relevant transcription factor and validate the identity through EMSA supershift analysis.


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 Mol. Cell. ProteomicsHome page
J. A. Stead, J. N. Keen, and K. J. McDowall
The Identification of Nucleic Acid-interacting Proteins Using a Simple Proteomics-based Approach That Directly Incorporates the Electrophoretic Mobility Shift Assay
Mol. Cell. Proteomics, September 1, 2006; 5(9): 1697 - 1702.
[Abstract] [Full Text] [PDF]


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